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Literature summary for 1.14.17.4 extracted from

  • Dilley, D.R.; Wang, Z.; Kadirjan-Kalbach, D.K.; Ververidis, F.; Beaudry, R.; Padmanabhan, K.
    1-Aminocyclopropane-1-carboxylic acid oxidase reaction mechanism and putative post-translational activities of the ACCO protein (2013), AoB plants, 5, plt031.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
2,4-pteridinediol i.e. lumazine, competitively activates the enzyme with respect to ascorbate Malus domestica
bicarbonate 20 mM bicarbonate pretreatment for 20 min is sufficient to protect and activate the enzyme Malus domestica
cyanide the enzyme is activated by cyanide concentrations between 0.1 and 1 mM with most efficient activation at 0.5 mM Malus domestica

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Malus domestica

Protein Variants

Protein Variants Comment Organism
C133A the mutant showsincreased activity compared to the wild type enzyme Malus domestica
C133P the mutant shows slightly increased activity compared to the wild type enzyme Malus domestica
C165A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
C28A the mutant shows increased activity compared to the wild type enzyme Malus domestica
E294F the mutant shows reduced activity compared to the wild type enzyme Malus domestica
E297L the mutant shows strongly increased activity compared to the wild type enzyme Malus domestica
E301D the mutant shows reduced activity compared to the wild type enzyme Malus domestica
E301L the mutant shows reduced activity compared to the wild type enzyme Malus domestica
F187Y the mutant shows increased activity compared to the wild type enzyme Malus domestica
F300Q the mutant shows reduced activity compared to the wild type enzyme Malus domestica
F300Y the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K144E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K158E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K158L the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K158Q the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K158Q/R175E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K158Q/R175Q the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K158R the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K158R/R175Q the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K172E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K199E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K230E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K230Q the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K230R the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K292E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K292R the mutant shows reduced activity compared to the wild type enzyme Malus domestica
K296E the mutant shows increased activity compared to the wild type enzyme Malus domestica
N216F the mutant shows reduced activity compared to the wild type enzyme Malus domestica
P298A the mutant shows strongly increased activity compared to the wild type enzyme Malus domestica
Q188A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
Q188K the mutant shows reduced activity compared to the wild type enzyme Malus domestica
Q188N the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175E the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175E/R244K the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175E/S246A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175E/T157A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175G the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175H the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175K the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R175Q the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R244K the mutant is less active than the native enzyme and has a 5fold higher Km value for 1-aminocyclopropane-1-carboxylate Malus domestica
R244K/S246A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R244K/S246A/T157A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R244K/T157A the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R299E inactive Malus domestica
R299H the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R299K the mutant shows reduced activity compared to the wild type enzyme Malus domestica
R299L the mutant shows reduced activity compared to the wild type enzyme Malus domestica
S246A the mutant is less active than the native enzyme and has a 3fold higher Km value for 1-aminocyclopropane-1-carboxylate Malus domestica
T157A the mutation does not affect the Km for 1-aminocyclopropane-1-carboxylate but drastically reduces enzyme activity Malus domestica
W203F the mutant shows reduced activity compared to the wild type enzyme Malus domestica
Y251F the mutant shows reduced activity compared to the wild type enzyme Malus domestica

Inhibitors

Inhibitors Comment Organism Structure
cyanide inhibitory beyond 1 mM Malus domestica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.031
-
1-aminocyclopropane-1-carboxylate mutant enzyme E301L, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.031
-
1-aminocyclopropane-1-carboxylate mutant enzyme R299L, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.036
-
1-aminocyclopropane-1-carboxylate mutant enzyme F300Y, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.046
-
1-aminocyclopropane-1-carboxylate mutant enzyme K158R, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.047
-
1-aminocyclopropane-1-carboxylate mutant enzyme R299K, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.051
-
1-aminocyclopropane-1-carboxylate wild type enzyme, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.06
-
1-aminocyclopropane-1-carboxylate mutant enzyme K158Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.062
-
1-aminocyclopropane-1-carboxylate mutant enzyme C28A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.062
-
1-aminocyclopropane-1-carboxylate mutant enzyme Y251F, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.063
-
1-aminocyclopropane-1-carboxylate mutant enzyme W203F, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.07
-
1-aminocyclopropane-1-carboxylate mutant enzyme T157A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.078
-
1-aminocyclopropane-1-carboxylate mutant enzyme K199E, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.083
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175K, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.09
-
1-aminocyclopropane-1-carboxylate mutant enzyme F187Y, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.094
-
1-aminocyclopropane-1-carboxylate mutant enzyme R299H, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.129
-
1-aminocyclopropane-1-carboxylate mutant enzyme F300Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.139
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175H, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.142
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175G, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.158
-
1-aminocyclopropane-1-carboxylate mutant enzyme N216F, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.173
-
1-aminocyclopropane-1-carboxylate mutant enzyme K158E, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.175
-
1-aminocyclopropane-1-carboxylate mutant enzyme R244K, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.175
-
1-aminocyclopropane-1-carboxylate mutant enzyme R244K/S246A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.193
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.206
-
1-aminocyclopropane-1-carboxylate mutant enzyme K158Q/R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.218
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.245
-
1-aminocyclopropane-1-carboxylate mutant enzyme R244K/S246A/T157A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.277
-
1-aminocyclopropane-1-carboxylate mutant enzyme S246A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.279
-
1-aminocyclopropane-1-carboxylate mutant enzyme K158R/R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.281
-
1-aminocyclopropane-1-carboxylate mutant enzyme K158L, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.287
-
1-aminocyclopropane-1-carboxylate mutant enzyme Q188N, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.379
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175E, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
0.659
-
1-aminocyclopropane-1-carboxylate mutant enzyme K158Q/R175E, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
1.2
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175E/S246A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica
2.3
-
1-aminocyclopropane-1-carboxylate mutant enzyme R175E/T157A, in 50 mM MOPS-HCl (pH 7.2), at 30°C Malus domestica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-aminocyclopropane-1-carboxylate + ascorbate + O2 Malus domestica
-
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
?

Organism

Organism UniProt Comment Textmining
Malus domestica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, column chromatography, and gel filtration Malus domestica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-aminocyclopropane-1-carboxylate + ascorbate + O2
-
Malus domestica ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
?
additional information the enzyme becomes inactivated by fragmentation and apparently has intrinsic protease and transpeptidase activity Malus domestica ?
-
?

Synonyms

Synonyms Comment Organism
1-aminocyclopropane-1-carboxylic acid oxidase
-
Malus domestica
ACC oxidase
-
Malus domestica
ACCO1
-
Malus domestica

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
Malus domestica

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the final step in ethylene biosynthesis. The enzyme is involved in the ethylene signal transduction pathway not directly linked to the enzyme reaction Malus domestica